Research workbench
E. cloacae mura dead-end complex with unag and fosfomycin
Analyse E. cloacae mura dead-end complex with unag and fosfomycin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LTH
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- EC
- 2.5.1.7
- UniProt
- P33038
- Ligands
- FFQ, UD1
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) | protein | 419 | 34% helix, 27% strand | P33038 |
Ligands and binding sites
- FFQ · [(1R)-1-hydroxypropyl]phosphonic acid · ligand · chains A
- UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.78 | 0.87 | 45 | FFQ, UD1 |
| 2 | 86 | 0.40 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 3LTH · E. cloacae MurA dead-end complex with UNAG and fosfomycin · the same entry in another collection · chain A against A, TM-score 1.00
- P33038 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P33038
- Elsewhere: RCSB PDB 3LTH · PDBe 3LTH · UniProt P33038
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